Cryptococcus neoformans Iron-Sulfur Protein Biogenesis Machinery Is a Novel Layer of Protection against Cu Stress

Autor: Sarela Garcia-Santamarina, Marta A. Uzarska, Richard A. Festa, Roland Lill, Dennis J. Thiele

Publikováno v: mBio, Vol 8, Iss 5 (2017)

ABSTRACT Copper (Cu) ions serve as catalytic cofactors to drive key biochemical processes, and yet Cu levels that exceed cellular homeostatic control capacity are toxic. The underlying mechanisms for Cu toxicity are poorly understood. During pulmonar

Externí odkaz: https://doaj.org/article/cf5d3641b1104700a491f77f81386edc

Mitochondrial Bol1 and Bol3 function as assembly factors for specific iron-sulfur proteins

Autor: Marta A Uzarska, Veronica Nasta, Benjamin D Weiler, Farah Spantgar, Simone Ciofi-Baffoni, Maria Rosaria Saviello, Leonardo Gonnelli, Ulrich Mühlenhoff, Lucia Banci, Roland Lill

Publikováno v: eLife, Vol 5 (2016)

Assembly of mitochondrial iron-sulfur (Fe/S) proteins is a key process of cells, and defects cause many rare diseases. In the first phase of this pathway, ten Fe/S cluster (ISC) assembly components synthesize and insert [2Fe-2S] clusters. The second

Externí odkaz: https://doaj.org/article/542cec6e518847f58ec908a4fd547ae8

Glutaredoxins and iron-sulfur protein biogenesis at the interface of redox biology and iron metabolism

Autor: Joseph J. Braymer, Ulrich Mühlenhoff, Roland Lill, Marta A. Uzarska, Benjamin D Weiler, Stefan Christ, Nicole Rietzschel

Publikováno v: Biological chemistry. 401(12)

The physiological roles of the intracellular iron and redox regulatory systems are intimately linked. Iron is an essential trace element for most organisms, yet elevated cellular iron levels are a potent generator and amplifier of reactive oxygen spe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a818f4f55d94fb522abd3f563d8ce995
https://pubmed.ncbi.nlm.nih.gov/33031050

Conserved functions of Arabidopsis mitochondrial late-acting maturation factors in the trafficking of iron‑sulfur clusters

Autor: Roland Lill, Flavien Zannini, Farah Spantgar, Ulrich Mühlenhoff, Nicolas Rouhier, Marta A. Uzarska, Jonathan Przybyla-Toscano

Publikováno v: Biochimica et Biophysica Acta-Molecular Cell Research
Biochimica et Biophysica Acta-Molecular Cell Research, Elsevier, 2018, 1865 (9), pp.1250-1259. ⟨10.1016/j.bbamcr.2018.06.003⟩

Numerous proteins require iron‑sulfur (Fe-S) clusters as cofactors for their function. Their biogenesis is a multi-step process occurring in the cytosol and mitochondria of all eukaryotes and additionally in plastids of photosynthetic eukaryotes. A

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b55c5d873e5b324785b8aacf5c3baf9
https://pubmed.ncbi.nlm.nih.gov/29902489

The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation

Autor: Sven-Andreas Freibert, Marta A. Uzarska, Rafal Dutkiewicz, Roland Lill, Ulrich Mühlenhoff

Publikováno v: Molecular Biology of the Cell

The monothiol glutaredoxin Grx5 is defined as a core member of mitochondrial Fe/S protein biogenesis. Grx5 undergoes a highly specific protein interaction with the dedicated Hsp70 chaperone Ssq1. The simultaneous presence of the scaffold protein Isu1

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0826796c6c4e5a26b4922b44af2483f3
http://europepmc.org/articles/PMC3681689